METTL2 forms a complex with the DALRD3 anticodon-domain binding protein to catalyze formation of 3-methylcytosine in specific arginine tRNA isoacceptors
Lentini, J. M.; Fu, D.
Show abstract
In mammals, a subset of arginine tRNA isoacceptors are methylated in the anticodon loop by the METTL2 methyltransferase to form the 3-methylcytosine (m3C) modification. However, the mechanism by which METTL2 identifies specific arginine tRNAs for m3C formation as well as the biological role of m3C in mammals is unknown. Here, we show that human METTL2 forms a complex with DALR anticodon binding domain containing 3 (DALRD3) protein in order to recognize particular arginine tRNAs destined for m3C modification. Using biochemical reconstitution, we find that METTL2-DALDR3 complexes catalyze m3C formation in vitro that is dependent upon sequence elements specific to certain arginine tRNAs. Notably, DALRD3-deficient human cells exhibit nearly complete loss of the m3C modification in arginine tRNAs. These findings uncover an unexpected function for the DALRD3 protein in the targeting of distinct arginine tRNAs for m3C modification.
Matching journals
The top 5 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Distinct functions for the paralogous RBM41 and U11/U12-65K proteins in the minor spliceosome 96%
- Reconstitution of the Human tRNA Splicing Endonuclease Complex: insight into the regulation of pre-tRNA cleavage. 96%
- Human NOP2/NSUN1 Regulates Ribosome Biogenesis Through Non-Catalytic Complex Formation with Box C/D snoRNPs. 95%
Similar papers in this journal
- Human TRMT1 and TRMT1L paralogs ensure the proper modification state, stability, and function of tRNAs 97%
- SAP30BP interacts with RBM17/SPF45 to promote splicing in a subset of human short introns 95%
- Numerous post-translational modifications of RNA polymerase II subunit Rpb4 link transcription to post-transcriptional mechanisms 94%
Similar papers in this journal
- tRNA m1G9 modification depends on substrate-specific RNA conformational changes induced by the methyltransferase Trm10 95%
- Crosstalk between the tRNA methyltransferase Trm1 and RNA chaperone La influences eukaryotic tRNA maturation 95%
- A non-canonical RNA-binding domain of the Fragile X protein, FMRP, elicits translational repression independent of mRNA G-quadruplexes 95%
Similar papers in this journal
- A comparison of Dictyostelium discoideum 3'-5' RNA polymerases reveals a conserved tRNAHis guanylyltransferase residue that plays a dual role in catalysis 95%
- Cytosolic RNA binding of the mitochondrial TCA cycle enzyme malate dehydrogenase (MDH2) 95%
- Structural and mechanistic insights into Dis3L2 mediated degradation of structured RNA 95%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.